23VY

Crystal structure of the mouse RORalpha ligand binding domain in fusion with an NRIP1 LXXLL peptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PAL/PLS BEAMLINE 7A (6B, 6C1)
Synchrotron site	PAL/PLS
Beamline	7A (6B, 6C1)
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-05-30
Detector	DECTRIS EIGER2 S 9M
Wavelength(s)	0.97950
Spacegroup name	C 1 2 1
Unit cell lengths	115.804, 75.775, 81.661
Unit cell angles	90.00, 119.04, 90.00

Refinement procedure

Resolution	34.200 - 2.700
R-factor	0.1882
Rwork	0.181
R-free	0.24900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.056
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.750
High resolution limit [Å]	2.700	2.700
Rmerge	0.067	0.381
Number of reflections	16980	852
<I/σ(I)>	30.7
Completeness [%]	99.7
Redundancy	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	9	297	0.1M HEPES-NaOH pH 9.0, 0.2M tri-sodium citrate, 5% propanol